Both N- and C-terminal Domains of RelB Are Required for Full Transactivation: Role of the N-terminal Leucine Zipper-like Motif

Overview

Journal Mol Cell Biol

Specialty Cell Biology

Date 1993 Mar 1

PMID 8441398

Citations 43

Authors

P Dobrzanski

R P Ryseck

R Bravo

Affiliations

Soon will be listed here.

Abstract

RelB, a member of the Rel family of transcription factors, can stimulate promoter activity in the presence of p50-NF-kappa B or p50B/p49-NF-kappa B in mammalian cells. Transcriptional activation analysis reveals that the N and C termini of RelB are required for full transactivation in the presence of p50-NF-kappa B. RelB/p50-NF-kappa B hybrid molecules containing the Rel homology domain of p50-NF-kappa B and the N and C termini of RelB have high transcriptional activity compared with wild-type p50-NF-kappa B. The N and C termini of RelB cooperate in transactivation in cis or trans configuration. Alterations in the structure of the leucine zipper-like motif present in the N terminus of RelB significantly decrease the transcriptional capacity of RelB and of different RelB/p50-NF-kappa B hybrid molecules.

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